Evolutionary Conserved Positions Define Protein Conformational Diversity.

ABSTRACT: Conformational diversity of the native state plays a central role in modulating protein function. The selection paradigm sustains that different ligands shift the conformational equilibrium through their binding to highest-affinity conformers. Intramolecular vibrational dynamics associated to each conformation should guarantee conformational transitions, which due to its importance, could possibly be associated with evolutionary conserved traits. Normal mode analysis, based on a coarse-grained model of the protein, can provide the required information to explore these features. Herein, we present a novel procedure to identify key positions sustaining the conformational diversity associated to ligand binding. The method is applied to an adequate refined dataset of 188 paired protein structu

SUBMITTER: Saldano TE 

PROVIDER: S-EPMC4805271 | biostudies-literature | 2016 Mar

REPOSITORIES: biostudies-literature